Purification and Properties of Leucine Aminopeptidase from Aspegillus japonica. II
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概要
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Leucine aminopeptidase was purified from culture filtrate of Aspergillus japonica by calcium acetate treatment, ammonium sulfate fractionation, and column chromatography with diethylaminoethyl (DEAE)-cellulose, Sephadex G-100 and CM-Sephadex C-50. The purified enzyme was homogeneous in disc electrophoretic analysis. Its molecular weight was estimated to be 57000 by Sephadex G-75 gel-filtration. The enzyme was most active at pH 8.0 towards L-leucylglycylglycine (Leu-Gly-Gly) and L-leucyl β-naphthylamide (Leu-β-NA), and its optimum temperature was 50°. The enzyme was stable in a pH range of 5.5 to 8.5 and below 50°. The purified enzyme was highly activated by Co^<2+> and was strongly inhibited by Fe^<3+>, Hg^<2+>, Cu^<2+>, Pb^<2+>, Ni^<2+>, ethylenediaminetetraaceticacid (EDTA), o-phenanthroline and N-bromosuccinimide. However, it was not affected by SH-reagents and diisopropyl fluorophosphate (DFP). The enzyme is considered to be leucine aminopeptidase, because it preferentially hydrolyzed di-or tripeptides with N-terminal leucine.
- 公益社団法人日本薬学会の論文
- 1976-09-25
著者
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杉浦 衛
Department of Pharmacy, Tokyo College of Pharmacy
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佐々木 正憲
Niigata College Of Pharmacy
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佐々木 正憲
Department of Pharmacy, Tokyo College of Pharmacy
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石川 正夫
東京薬科大学
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鈴木 睦子
東京薬科大学
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鈴木 睦子
Department of Pharmacy, Tokyo College of Pharmacy
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石川 正夫
Department of Pharmacy, Tokyo College of Pharmacy
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佐々木 正憲
Department Of Pharmacology And Pharmacy Niigata College Of Pharmacy
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